Calcium Binding by Arabinogalactan Polysaccharides Is Important for Normal Plant Development

Lopez-Hernandez, Federico; Tryfona, Theodora; Rizza, Annalisa; Yu, Xiaolan; Harris, Matthew; Webb, Alex A. R.; Kotake, Toshihisa; Dupree, Paul

doi:10.1105/tpc.20.00027

Cited by 71 publications

(79 citation statements)

References 122 publications

(186 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…AtGLCAT14 mutants have defective synthesis of AGs. glcat14a,glcat14b,glcat14d,glcat14e,glcat14aglcat14b,glcat14bglcat14c,glcat14aglcat14bglcat14c,glcat14aglcat14bglcat14d, and glcat14aglcat14bglcat14e mutants have reduced the content of GlcA on AGPs when compared to wild type (Knoch et al, 2013;Lopez-Hernandez et al, 2020;Zhang et al, 2020). Although this suggests some redundancy between these enzymes, the mutants show some preferential changes in GlcA on specific branch lengths of AG and, therefore, may have roles glucuronidating different parts of the AG or different AGPs (Lopez-Hernandez et al, 2020).…”

Section: Glucuronosyltransferases: Adding the Special Sugarmentioning

confidence: 97%

“…The biosynthesis of AGP glycans requires at least 10 functionally distinct enzymes, e.g., galactosyltransferases (GALTs), arabinosyltransferases, fucosyltransferases (FUTs), rhamnosyltransferases, xylosyltransferases, glucuronosyltransferases 1 http://www.cazy.org (GLCATs), and glucuronic acid methyltransferases. To date, 22 transferases responsible for AGP glycosylation have been identified in Arabidopsis (Tables 1 and 2): eight hydroxyproline-O-β-GALTs (Hyp-O-GALTs; AtGALT2, AtGALT3, AtGALT4, AtGALT5, and AtGALT6, Basu et al, 2013Basu et al, , 2015aShowalter and Basu, 2016;AtHPTG1, AtHPTG2, and AtHPTG3, Ogawa-Ohnishi and Matsubayashi, 2015), two β-1,3-GALTs (At1g77810, Qu et al, 2008 andAtKSN4, Suzuki et al, 2017), two β-1,6-GALTs (AtGALT31A, Geshi et al, 2013 and AtGALT29A;, five β-1,6-GLCATs (AtGLCAT14A, AtGLCAT14B, AtGLCAT14C, AtGLCAT14D, and AtGLCAT14E, Knoch et al, 2013;Lopez-Hernandez et al, 2020;Zhang et al, 2020), two α-1,2-FUTs (AtFUT4 and AtFUT6, Wu et al, 2010;Liang et al, 2013;Tryfona et al, 2014), a putative β-arabinosyltransferase (AtRAY1, Gille et al, 2013), and two glucuronic acid methyltransferases (AtAGM1 and AtAGM2, Temple et al, 2019; Figure 3). However, several enzymes remain to be identified, including α-arabinofuranosyltransferases, β-arabinopyranosyltransferases, α-rhamnosyltransferases, α-xylosyltransferases, an α-GALTs, and other β-GALTs, β-GLCATs, α-FUTs, and glucuronic acid methyltransferases.…”

Section: Glycosyltransferases: Meet the Sugar Workersmentioning

confidence: 99%

“…AtGLCAT14A was transiently expressed in N. benthamiana and localized in the Golgi apparatus. AtGLCAT14A is co-localized with AtGALT31A in the Golgi and in -2, glcat14b-1, glcat14d-1, glcat14e-1, glcat14aglcat14b, glcat14a-2/b-1, glcat14bglcat14c, glcat14aglcat14bglcat14c, glcat14a-2/b-1/d-1, glcat14a-2/b-1/d-2, and glcat14a-2/b-1/e-1); increase of Gal and Ara in AGPs (glcat14c, glcat14aglcat14b, glcat14bglcat14c, and glcat14aglcat14bglcat14c); reduction of Ara in AGPs (glcat14a-1 and glcat14a-2); reduced amount of glycosylated AGPs (glcat14c, glcat14aglcat14b, and glcat14aglcat14bglcat14c); reduction in Ca 2+ binding capacity of AGPs (glcat14b,glcat14c,glcat14aglcat14b,glcat14bglcat14c,glcat14aglcat14bglcat14c,; enhanced cell elongation in seedlings (glcat14a-1 and glcat14a-2); reduced seed coat mucilage (glcat14b, glcat14c, glcat14aglcat14b, glcat14bglcat14c, and glcat14aglcat14bglcat14c); delayed seed germination and reduced root hair length (glcat14aglcat14b and glcat14aglcat14bglcat14c); reduced trichome branching ( glcat14aglcat14b, glcat14a-2/b-1, glcat14aglcat14bglcat14c, glcat14a-2/b-1/d-1, and glcat14a-2/b-1/d-2); shorter siliques and reduced seed production (glcat14bglcat14c and glcat14aglcat14bglcat14c); small and defective pollen that failed to germinate (glcat14aglcat14b and glcat14aglcat14bglcat14c); shorter inflorescence stems (glcat14a-2/b-1 and glcat14a-2/b-1/d-1); smaller etiolated hypocotyls and altered [Ca 2+ ]cyt signature on roots (glcat14a-2/b-1/e-1) Knoch et al, 2013;Lopez-Hernandez et al, 2020;Zhang et al, 2020…”

Section: Glucuronosyltransferases: Adding the Special Sugarmentioning

confidence: 99%

“…AtGLCAT14 mutants present several phenotypes. glcat14a knockout mutants showed enhanced cell elongation during seedling growth (Knoch et al, 2013), glcat14b, glcat14c, glcat14aglcat14b, glcat14bglcat14c, and glcat14aglcat14bglcat14c presented reduced seed coat mucilage, glcat14aglcat14b and glcat14aglcat14bglcat14c exhibited delayed seed germination, reduced root hair length, glcat14aglcat14b, glcat14aglcat14bglcat14c, and glcat14aglcat14bglcat14d reduced trichome branching, glcat14aglcat14b and glcat14aglcat14bglcat14d presented shorter inflorescences, glcat14bglcat14c and glcat14aglcat14bglcat14c presented reduced silique length and seed set, and glcat14aglcat14b and glcat14aglcat14bglcat14c displayed a significant percentage of small and defective pollen that failed to germinate (Lopez-Hernandez et al, 2020;Zhang et al, 2020). glcat14aglcat14bglcat14e triple mutant plants had severely limited seedling growth and were sterile (Lopez-Hernandez et al, 2020).…”

Section: Glucuronosyltransferases: Adding the Special Sugarmentioning

confidence: 99%

See 3 more Smart Citations

Three Decades of Advances in Arabinogalactan-Protein Biosynthesis

et al. 2020

Self Cite

View full text Add to dashboard Cite

Arabinogalactan-proteins (AGPs) are a large, complex, and highly diverse class of heavily glycosylated proteins that belong to the family of cell wall hydroxyproline-rich glycoproteins. Approximately 90% of the molecules consist of arabinogalactan polysaccharides, which are composed of arabinose and galactose as major sugars and minor sugars such as glucuronic acid, fucose, and rhamnose. About half of the AGP family members contain a glycosylphosphatidylinositol (GPI) lipid anchor, which allows for an association with the outer leaflet of the plasma membrane. The mysterious AGP family has captivated the attention of plant biologists for several decades. This diverse family of glycoproteins is widely distributed in the plant kingdom, including many algae, where they play fundamental roles in growth and development processes. The journey of AGP biosynthesis begins with the assembly of amino acids into peptide chains of proteins. An N-terminal signal peptide directs AGPs toward the endoplasmic reticulum, where proline hydroxylation occurs and a GPI anchor may be added. GPI-anchored AGPs, as well as unanchored AGPs, are then transferred to the Golgi apparatus, where extensive glycosylation occurs by the action of a variety glycosyltransferase enzymes. Following glycosylation, AGPs are transported by secretory vesicles to the cell wall or to the extracellular face of the plasma membrane (in the case of GPI-anchored AGPs). GPI-anchored proteins can be released from the plasma membrane into the cell wall by phospholipases. In this review, we present an overview of the accumulated knowledge on AGP biosynthesis over the past three decades. Particular emphasis is placed on the glycosylation of AGPs as the sugar moiety is essential to their function. Recent genetics and genomics approaches have significantly contributed to a broader knowledge of AGP biosynthesis. However, many questions remain to be elucidated in the decades ahead.

show abstract

Section: Glucuronosyltransferases: Adding the Special Sugarmentioning

confidence: 97%

Section: Glycosyltransferases: Meet the Sugar Workersmentioning

confidence: 99%

Section: Glucuronosyltransferases: Adding the Special Sugarmentioning

confidence: 99%

Section: Glucuronosyltransferases: Adding the Special Sugarmentioning

confidence: 99%

See 2 more Smart Citations

Three Decades of Advances in Arabinogalactan-Protein Biosynthesis

et al. 2020

Self Cite

View full text Add to dashboard Cite

show abstract

“…Moreover, the Ca 2+capacitor hypothesis does not exclude any other roles of type II AG. At any rate, the Ca 2+ -capacitor hypothesis is so far supported at the genetic level by mutant plants lacking several type II AG specific glucuronyl transferases (Knoch et al, 2013;Lopez-Hernandez et al, 2020;Zhang et al, 2020).…”

Section: What Is the Function Of Type II Arabinogalactan O-linked Glymentioning

confidence: 99%

On the Potential Function of Type II Arabinogalactan O-Glycosylation in Regulating the Fate of Plant Secretory Proteins

Seifert

2020

Front. Plant Sci.

View full text Add to dashboard Cite

In a plant-specific mode of protein glycosylation, various sugars and glycans are attached to hydroxyproline giving rise to a variety of diverse O-glycoproteins. The sub-family of arabinogalactan proteins is implicated in a multitude of biological functions, however, the mechanistic role of O-glycosylation on AGPs by type II arabinogalactans is largely elusive. Some models suggest roles of the O-glycans such as in ligand-receptor interactions and as localized calcium ion store. Structurally different but possibly analogous types of protein O-glycosylation exist in animal and yeast models and roles for O-glycans were suggested in determining the fate of O-glycoproteins by affecting intracellular sorting or proteolytic activation and degradation. At present, only few examples exist that describe how the fate of artificial and endogenous arabinogalactan proteins is affected by O-glycosylation with type II arabinogalactans. In addition to other roles, these glycans might act as a molecular determinant for cellular localization and protein lifetime of many endogenous proteins.

show abstract

Different responses of banana classical AGP genes and cell wall AGP components to low-temperature between chilling sensitive and tolerant cultivars

et al. 2022

View full text Add to dashboard Cite

Classical arabinogalactan proteins (AGPs) belong to glycosylphosphatidylinositol-anchored proteins, which are proved to be involved in signaling and cell wall metabolism upon stresses. However, rare information is available on the roles of classical AGPs in low temperature (LT) tolerance. Cultivation of banana in tropical and subtropical region is seriously threatened by LT stress. In the present study, 17 classical MaAGPs and nine MbAGPs in banana A and B genome were identi ed and characterized, respectively. Great diversity was present among different classical MaAGP/MbAGP members while ve members (AGP3/6/11/13/14) showed 100% identity between these two gene families. We further investigated different responses of classical AGPs to LT between a chilling sensitive (CS) and tolerant (CT) banana cultivars. In addition, different changes in the temporal and spatial distribution of cell wall AGP components under LTs between these two cultivars were compared using immuno uorescence labeling. Seven classical MbAGPs were upregulated by LT(s) in the CT cultivar. Classical MaAGP4/6 was induced by LT(s) in both cultivars while MaAGP1/2/9/16/17 only in the CT cultivar. Moreover, these genes showed signi cantly higher transcription abundance in the CT cultivar than the CS one under LT(s) except classical MaAGP4. Similar results were observed with the epitopes of JIM13 and LM2 antibodies. The antigens of these antibodies and classical MaAGP1/2/6/9/16/17 might be related to LT tolerance of banana. These results provide additional information about plant classical AGPs and their involvement in LT tolerance, as well as their potential as candidate genes to be targeted when breeding CT banana. Key MessageSeven-teen classical MaAGPs and nine MbAGPs were identi ed and analyzed. MaAGP1/2/6/9/16/17, the antigens of JIM13 and LM2 antiboides are likely to be involved in banana chilling tolerance.

show abstract

Calcium Binding by Arabinogalactan Polysaccharides Is Important for Normal Plant Development

Cited by 71 publications

References 122 publications

Three Decades of Advances in Arabinogalactan-Protein Biosynthesis

Three Decades of Advances in Arabinogalactan-Protein Biosynthesis

On the Potential Function of Type II Arabinogalactan O-Glycosylation in Regulating the Fate of Plant Secretory Proteins

Different responses of banana classical AGP genes and cell wall AGP components to low-temperature between chilling sensitive and tolerant cultivars

Contact Info

Product

Resources

About